Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding.

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Article

Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding.

The Journal of biological chemistry - 25 Sept 1990

Gomi T, Takata Y, Date T, Fujioka M, Aksamit R R, Backlund P S, Cantoni G L

Abstract excerpt

Aspartic acid 244 that occurs at the putative NAD(+)-binding site of rat liver S-adenosylhomocysteinase was replaced by glutamic acid by oligonucleotide-directed mutagenesis. The mutant enzyme was purified to homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Gel...

Topics

Adenosylhomocysteinase
Apoenzymes
Aspartic Acid
Base Sequence
Binding Sites
Cloning, Molecular
Escherichia coli
Glutamates
Glutamic Acid
Hydrolases
Kinetics
Liver

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Molecular Weight

Mutation

NAD

Oligonucleotide Probes

Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 1975808

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1975808-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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